Studies of Human Kidney and Urine Acid Phosphatase

Enzyme ◽  
1971 ◽  
Vol 12 (3) ◽  
pp. 257-268 ◽  
Author(s):  
H.J. Kramer ◽  
H.C. Gonick
Keyword(s):  
Acid Phosphatase ◽  
Human Kidney

Studies of Human Kidney and Urine Acid Phosphatase

1970 ◽  
Vol 11 (5) ◽  
pp. 435-449 ◽  
Author(s):  
H.J. Kramer ◽  
J.E. Wight ◽  
W.L. Paul ◽  
H.C. Gonick
Keyword(s):  
Acid Phosphatase ◽  
Human Kidney

Development and evaluation of a new solid-phase direct immunoenzyme assay for prostatic acid phosphatase.

1982 ◽  
Vol 28 (4) ◽  
pp. 596-602 ◽  
Author(s):  
K Gericke ◽  
K P Kohse ◽  
G Pfleiderer ◽  
S H Flüchter ◽  
K H Bichler
Keyword(s):  
Acid Phosphatase ◽  
Prostatic Cancer ◽  
Solid Phase ◽  
Human Kidney ◽  
Prostatic Acid Phosphatase ◽  
Enzymic Activity ◽  
Organ Specificity ◽  
Polystyrene Tube ◽  
Prostatic Diseases ◽  
Independent Distribution

Abstract In this assay we used polystyrene-tube-attached rabbit antibodies against prostatic acid phosphatase (PAP) that had been purified to homogeneity from human prostate. The amount of immunoreactive acid phosphatase was determined directly by its enzymic activity in the solid-phase-bound immune complex. The detection limit was 0.05 U/L (0.13 microgram/L), the CVs between 4.3 and 10.8%. Investigating the organ specificity of PAP, we found that some cross-reacting acid phosphatase activity could be so measured in human kidney, leukocytes, and platelets, all of which probably contribute to the circulating "prostatic" acid phosphatase that normally is present in serum. Diurnal and day-to-day variations in serum PAP activity were as much as 100% in healthy subjects. Individuals without prostatic diseases (n = 92) had values for serum PAP activity up to 0.36 U/L (0.94 microgram/L), in an age-independent distribution; patients with benign prostatic hyperplasia (n = 62) showed values up to 0.48 U/L (1.25 micrograms/L). With PAP activity of 0.38 U/L or 1.0 microgram/L (90th percentile of the prostatic group) as the upper limit of "normality," overall sensitivity (stages A-D) for detection of prostatic cancer in 33 essentially untreated patients was 65%. Examples for the followup of therapy of prostatic cancer by measurement of serum PAP with this assay are described.

Erythrophagocytosis in the Liver in Hemolytic Anemias

1968 ◽  
Vol 26 ◽  
pp. 184-185
Author(s):  
O. T. Minick ◽  
E. Orfei ◽  
F. Volini ◽  
G. Kent
Keyword(s):  
Acid Phosphatase ◽  
Oxidative Damage ◽  
Phosphatase Activity ◽  
Kupffer Cells ◽  
Acid Phosphatase Activity ◽  
Common Type ◽  
Red Cell ◽  
Cell Fragments ◽  
Reticulo Endothelial System ◽  
Important Site

Hemolytic anemias were produced in rats by administering phenylhydrazine or anti-erythrocytic (rooster) serum, the latter having agglutinin and hemolysin titers exceeding 1:1000.Following administration of phenylhydrazine, the erythrocytes undergo oxidative damage and are removed from the circulation by the cells of the reticulo-endothelial system, predominantly by the spleen. With increasing dosage or if animals are splenectomized, the Kupffer cells become an important site of sequestration and are greatly hypertrophied. Whole red cells are the most common type engulfed; they are broken down in digestive vacuoles, as shown by the presence of acid phosphatase activity (Fig. 1). Heinz body material and membranes persist longer than native hemoglobin. With larger doses of phenylhydrazine, erythrocytes undergo intravascular fragmentation, and the particles phagocytized are now mainly red cell fragments of varying sizes (Fig. 2).

The Demonstration of Human Prostatic Acid Phosphatase (Pap) With Phosphorylcholine

1976 ◽  
Vol 34 ◽  
pp. 88-89
Author(s):  
José A. Serrano ◽  
Hannah L. Wasserkrug ◽  
Anna A. Serrano ◽  
Arnold M. Seligman
Keyword(s):  
Acid Phosphatase ◽  
Prostate Gland ◽  
Prostatic Acid Phosphatase ◽  
Human Prostate ◽  
Rat Tissues ◽  
Specific Substrate ◽  
Acid Phosphatases ◽  
Lysosomal Acid ◽  
Cacodylate Buffer

As previously reported (1, 2) phosphorylcholine (PC) is a specific substrate for prostatatic acid phosphatase (PAP) as opposed to other acid phosphatases, e.g., lysosomal acid phosphatase. The specificity of PC for PAP is due to the pentavalent nitrogen in PC, a feature that renders PC resistant to hydrolysis by all other acid phosphatases. Detailed comparative cytochemical results in rat tissues are in press. This report deals with ultracytochemical results applying the method to normal and pathological human prostate gland.Fresh human prostate was obtained from 7 patients having transurethral resections or radical prostatectomies. The tissue was fixed in 3% glutaraldehyde- 0.1 M cacodylate buffer (pH 7.4) for 15 min, sectioned at 50 μm on a Sorvall TC-2 tissue sectioner, refixed for a total of 2 hr, and rinsed overnight in 0.1 M cacodylate buffer (pH 7.4)-7.5% sucrose.

Prostatic Acid Phosphatase (PAP) Differentiated Ultracytochemically from Lysosomal Acid Phosphate in the Rat with a PAP/Specific Substrate, Phosphorylcholine

1975 ◽  
Vol 33 ◽  
pp. 450-451
Author(s):  
W. Allen Shannon ◽  
José A. Serrano ◽  
Hannah L. Wasserkrug ◽  
Anna A. Serrano ◽  
Arnold M. Seligman
Keyword(s):  
Acid Phosphatase ◽  
Phosphate Buffer ◽  
Prostatic Carcinoma ◽  
Prostatic Acid Phosphatase ◽  
Chemotherapeutic Agents ◽  
Specific Substrate ◽  
Acid Phosphate ◽  
Lysosomal Acid ◽  
Design And Synthesis ◽  
New Chemotherapeutic Agents

During the design and synthesis of new chemotherapeutic agents for prostatic carcinoma based on phosphorylated agents which might be enzyme-activated to cytotoxicity, phosphorylcholine, [(CH3)3+NCH2CH2OPO3Ca]Cl-, has been indicated to be a very specific substrate for prostatic acid phosphatase (PAP). This phenomenon has led to the development of specific histochemical and ultracytochemical methods for PAP using modifications of the Gomori lead method for acid phosphatase. Comparative histochemical results in prostate and kidney of the rat have been published earlier with phosphorylcholine (PC) and β-glycerophosphate (βGP). We now report the ultracytochemical results.Minced tissues were fixed in 3% glutaraldehyde-0.1 M phosphate buffered (pH 7.4) for 1.5 hr and rinsed overnight in several changes of 0.05 M phosphate buffer (pH 7.0) containing 7.5% sucrose. Tissues were incubated 30 min to 2 hr in Gomori acid phosphatase medium (2) containing 0.1 M substrate, either PC or βGP.

Integrated morphometrical and electron energy loss image analysis in cytochemistry

1989 ◽  
Vol 47 ◽  
pp. 402-403
Author(s):  
W.C. de Bruijn ◽  
A.A.W. de Jong ◽  
C.W.J. Sorber
Keyword(s):  
Image Analysis ◽  
Acid Phosphatase ◽  
Chemical Analysis ◽  
Active Form ◽  
List Type ◽  
Type Number ◽  
Enzyme Cytochemistry ◽  
Related Data ◽  
Endogenous Peroxidase ◽  
Electron Energy Loss

One aspect of enzyme cytochemistry is, whether all macrophage lysosomal hydrolytical enzymes are present in an active form, or are activated upon stimulation. Integrated morphometrical and chemical analysis has been chosen as a tool to illucidate that cytochemical problem. Mouse peritoneal resident macrophages have been used as a model for this complicated integration of morphometrical and element-related data. Only aldehyde-fixed cells were treated with three cytochemical reactions to detect different enzyme activities within one cell (for details see [1,2]). The enzyme-related precipitates anticipated to be differentiated, were:(1).lysosomal barium and sulphur from aryl sulphatase activity,(2).lysosomal cerium and phosphate from acid phosphatase activity and(3).platinum/di-amino-benzidine( D A B) complex from endogenous peroxidase activity.

vitreal cells and specialized phagocytes in the chick embryo retina: A TEM and SEM study

1990 ◽  
Vol 48 (3) ◽  
pp. 330-331
Author(s):  
M.A. Cuadros ◽  
M.J. Martinez-Guerrero ◽  
A. Rios
Keyword(s):  
Cell Death ◽  
Plasma Membrane ◽  
Acid Phosphatase ◽  
Chick Embryo ◽  
Basement Membrane ◽  
Sem Images ◽  
Intimate Contact ◽  
Cellular Processes ◽  
Sem Study ◽  
Free Cells

In the chick embryo retina (days 3-4 of incubation), coinciding with an increase in cell death, specialized phagocytes characterized by intense acid phosphatase activity have been described. In these preparations, all free cells in the vitreal humor (vitreal cells) were strongly labeled. Conventional TEM and SEM techniques were used to characterize them and attempt to determine their relationship with retinal phagocytes.Two types of vitreal cells were distinguished. The first are located at some distance from the basement membrane of the neuroepithelium, and are rounded, with numerous vacuoles and thin cytoplasmic prolongations. Images of exo- and or endocytosis were frequent; the cells showed a well-developed Golgi apparatus (Fig. 1) In SEM images, the cells was covered with short cellular processes (Fig. 3). Cells lying parallel to or alongside the basement membrane are elongated. The plasma membrane is frequently in intimate contact with the basement membrane. These cells have generally a large cytoplasmic expansion (Fig. 5).

Studies of Vegetative Plant Tissue Compatibility/Incompatibility: The Role of Acid Phosphatase in Lethal Cell Senescence in an Incompatible Heterograft

1980 ◽  
Vol 38 ◽  
pp. 530-531
Author(s):  
Randy Moore
Keyword(s):  
Acid Phosphatase ◽  
Thick Layer ◽  
Cell Necrosis ◽  
Enzyme Localization ◽  
Vegetative Plant ◽  
Cell Autolysis ◽  
Graft Interface ◽  
System 1 ◽  
Thin Fibril

Previous work has indicated that the graft incompatihility between Sedrmi telephoides and Solanum pennellil involves cell necrosis that results In a thick layer of collapsed cells at the graft Interface. This necrotic layer insulates the stock from the scion, which results in abscission of the Sedum scion after 4-6 weeks due to desiccation and starvation. Thus, cell autolysis (which is restricted to Sedum) characterizes the Incompatibility response in this system (1). In order to elucidate the events that lead to cell autolysis, and thus better understand the cellular site and mode of action of cellular incompatibility, the appearance and fate of the hydrolytlc enzyme acid phosphatase (AP) was followed in both the compatible Sedum autograft and the incompatible Sedum/Solanum heterograft. Acid phosphatase was localized by a modified Gomori-type reaction; positive (i.e., including NaF inhibitor) and negative (lacking substrate) controls showed no enzymatic precipitate. Following an initial association with the endoplasmic reticulum (ER) and dictyosomes at 6-10 hours after grafting, AP activity in the compatible Sedum autograft is associated primarily with the plasmalemma (Fig. 1). By 18-24 hours after grafting, the AP activity is restricted to the tono-plast and vacuole (Fig. 2). This strict compartmentation and absence of enzyme from the cytosol is maintained throughout the development of the compatible graft. While AP activity in the incompatible Sedum/Solanum heterograft is Initially similar to the compatible Sedum autograft (i.e., initially found on the ER and dictyosomes), there is a marked difference in enzyme localization in the two graft partners as the incompatibility response develops. As in the compatible autograft, Solanum cells at the graft interface show an Increase in AP activity that Is restricted to the vacuole and tonoplast, with little or no enzyme activity in the cytosol (Fig. 3). In comparable Sedum cells, however, there is a dramatic Increase In AP activity in the cytosol (Fig. h); this cytosollc AP activity is associated with thin fibril-like structures (Fig. 5) measuring approximately 60 A in diameter. This high cytoplasmic AP activity In Sedum cells results in cell autolysis, death, and eventual cell collapse to form the characteristic necrotic layer separating the two graft partners.

Histochemical and Ultrastructural Studies of the Digestive Epithelium in a Gastropod Gametolytic Organ

1980 ◽  
Vol 38 ◽  
pp. 568-569
Author(s):  
R. L. Reeder ◽  
S. H. Rogers ◽  
W. A. Shannon
Keyword(s):  
Acid Phosphatase ◽  
Genital Tract ◽  
Reproductive Tract ◽  
Ultrastructural Level ◽  
Conclusive Evidence ◽  
Digestive Organ ◽  
Limited Information ◽  
Ultrastructural Studies ◽  
Morphological Studies

Numerous morphological studies have dealt with the spermatheca of pulmonate gastropods. This globular organ, which is attached to the female portion of the reproductive tract by a long duct in these monoecious animals, has had various functions ascribed to it. Recent histochemical demonstrations of deoxyribonuclease, ribonuclease, protease, and acid phosphatase have provided, however, conclusive evidence that it is a digestive organ for the degradation of superfluous sperm and genital tract secretions. Only limited information concerning the spermatheca is available at the ultrastructural level, a fact providing the stimulus for the present study of this organ in Sonorella santaritana, a desert mountain snail from Arizona.

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